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Conformational dissection of Thermomyces lanuginosus lipase in solution.
Gonçalves, Karen M; Barbosa, Leandro R S; Lima, Luís Maurício T R; Cortines, Juliana R; Kalume, Dário E; Leal, Ivana C R; Mariz e Miranda, Leandro S; de Souza, Rodrigo O M; Cordeiro, Yraima.
Afiliación
  • Gonçalves KM; Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil; Instituto de Química, Universidade Federal do Rio de Janeiro, Centro de Tecnologia, Rio de Janeiro, RJ, Brazil.
  • Barbosa LR; Instituto de Física, Universidade de São Paulo, SP, Brazil.
  • Lima LM; Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil; Laboratory for Structural Biology (DIMAV), Brazilian National Institute of Metrology, Quality and Technology-INMETRO, Duque de Caxias, RJ 25250-020, Brazil.
  • Cortines JR; Departamento de Virologia, Instituto de Microbiologia Paulo de Góes, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-590, Brazil.
  • Kalume DE; Laboratório Interdisciplinar de Pesquisas Médicas, Instituto Oswaldo Cruz, Fundação Oswaldo Cruz, Rio de Janeiro, RJ 21040-360, Brazil.
  • Leal IC; Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil.
  • Mariz e Miranda LS; Instituto de Química, Universidade Federal do Rio de Janeiro, Centro de Tecnologia, Rio de Janeiro, RJ, Brazil.
  • de Souza RO; Instituto de Química, Universidade Federal do Rio de Janeiro, Centro de Tecnologia, Rio de Janeiro, RJ, Brazil.
  • Cordeiro Y; Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil. Electronic address: yraima@pharma.ufrj.br.
Biophys Chem ; 185: 88-97, 2014 Jan.
Article en En | MEDLINE | ID: mdl-24382361
Lipases are triacyl glycerol acyl hydrolases, which catalyze hydrolysis of esters, esterification and transesterification reactions, among others. Some of these enzymes have a large hydrophobic pocket covered by an alpha-helical mobile surface loop (the lid). Protein-protein interactions can occur through adsorption of two open lids of individual lipases. We investigated the conformation and oligomeric state of Thermomyces lanuginosus lipase (TLL) in solution by spectroscopic and mass spectrometry techniques. Information about oligomerization of this important industrial enzyme is only available for TLL crystals; therefore, we have done a throughout investigation of the conformation of this lipase in solution. SDS-PAGE and mass spectrometry analysis of size-exclusion chromatography eluted fractions indicated the presence of both monomeric and dimeric populations of TLL. The stability of the enzyme upon thermal and guanidine hydrochloride treatment was examined by circular dichroism and fluorescence emission spectroscopy. Small angle x-ray scattering and ion mobility mass spectrometry analysis revealed that TLL is found as a mixture of monomers and dimers at the assayed concentrations. Although previous x-ray diffraction data showed TLL as a dimer in the crystal (PDB: 1DT3), to our knowledge our report is the first evidencing that TLL co-exists as stable dimeric and monomeric forms in solution.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ascomicetos / Lipasa Idioma: En Revista: Biophys Chem Año: 2014 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Países Bajos
Texto completo
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Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ascomicetos / Lipasa Idioma: En Revista: Biophys Chem Año: 2014 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Países Bajos